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J. Virol., Jun 1997, 4852-4856, Vol 71, No. 6
PC Tai, D Banik, GI Lin, S Pai, K Pai, MH Lin, G Yuoh, S Che, SH Hsu, TC Chen, TT Kuo, CS Lee, CS Yang and C Shih
We examined the full-length hepatitis B virus (HBV) envelope (surface
antigen or HBV small surface antigen [HBsAg]) sequences of 12 different
liver samples from 10 different hepatoma-containing chronic carriers.
Surprisingly, novel and frequent mutations occurred predominantly at amino
acids 40 and 47 of HBsAg, in addition to within a known protective B-cell
epitope (so-called group a determinant of HBsAg 124- 148). Approximately
58% of chronic carriers contain mutations at the group a determinant. The
mutation frequency at the hotspot codons 40 and 47 is approximately 83%, 1
order of magnitude higher than at the known polymorphic sites of
subtype-specific determinants at codons 122 and 160, which is approximately
4%. This new mutational domain is found to coincide with a major
histocompatibility complex class I-restricted T-cell epitope. The potential
biological significance of this novel mutation in the immunopathogenesis of
HBV chronic carriers is discussed.
Copyright © 1997, American Society for Microbiology
Novel and frequent mutations of hepatitis B virus coincide with a major histocompatibility complex class I-restricted T-cell epitope of the surface antigen
Department of Pathology, WHO Collaborating Center for Tropical Diseases, University of Texas Medical Branch, Galveston 77555-0609, USA.
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